ID A0A084QCK5_STAC4 Unreviewed; 627 AA.
AC A0A084QCK5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN ORFNames=S40285_03462 {ECO:0000313|EMBL:KFA61690.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA61690.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA61690.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA61690.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000948};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363037}.
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DR EMBL; KL660839; KFA61690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QCK5; -.
DR STRING; 1283841.A0A084QCK5; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; A0A084QCK5; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR NCBIfam; TIGR00440; glnS; 1.
DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363037};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363037};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 89..400
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 404..499
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 512..569
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 15..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 71578 MW; 84A29376836705A2 CRC64;
MAEAVTQSVA KLQLDEETGE MVSKAELKKR QQKRAKKALQ EKARAEKAAA GPQDKPAPKA
KVEEAPIDPD AMFKQGFLEE VYKERPSEKV VTRFPPEPNG YLHIGHAKAI AVNFGFARHH
GGVCYLRYDD TNPEKEEEVY FTAIKDIVEW LGFKPFKITY SSDNFQRLYD LAEKLITMEK
AYVCACNDTE IKLQRGGEKG ATPRYRCSHA EQPVEENLTK FRDMRDGKYK PKEVFLRMKQ
DITSGNPQEW DLAAYRIKTD TPHHRTGWDW KIYPTYDFTH CLCDSFEGIT HSLCTTEFIM
SRVSYEWLNK TLGVYEPMQR EYGRLNLTGT VLSKRKILKL VEEKFVRSWD DPRLYSLIAI
RRRGVPPGAI LEFVNELGVT TSTTTIKIHR FEQSIRKYLE MTVPRLMMVL DPVPLVIEDA
EAVDVELPFS PKDPKMGSHK VRFTPTIYID RSDFREEDSK DFFRLAPGKT VGLLNAPYPV
KATSFTKDEA TGKVTEIRGV FDKETKKAKT YIQWVGTEGS RKVEARIHNA LFKSEKPEDA
EGGFLNDINP DSEIIYADAL LESGFDEVKR RAPWPEAAGE NELGKGGPES IRFQAMRVAY
FAVDSDSTDD KIVLNRIVSL KEDAGKK
//